3cbh
From Proteopedia
(New page: 200px<br /><applet load="3cbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="3cbh, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:3cbh.jpg|left|200px]]<br /><applet load="3cbh" size=" | + | [[Image:3cbh.jpg|left|200px]]<br /><applet load="3cbh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="3cbh, resolution 2.0Å" /> | caption="3cbh, resolution 2.0Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The enzymatic degradation of cellulose is an important process, both | + | The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase. The active site of CBHII is located at the carboxyl-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the center of the tunnel are the probable catalytic residues. |
==About this Structure== | ==About this Structure== | ||
| - | 3CBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http:// | + | 3CBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CBH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hypocrea jecorina]] | [[Category: Hypocrea jecorina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:08:42 2008'' |
Revision as of 17:08, 21 February 2008
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THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI
Overview
The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase. The active site of CBHII is located at the carboxyl-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the center of the tunnel are the probable catalytic residues.
About this Structure
3CBH is a Single protein structure of sequence from Hypocrea jecorina. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei., Rouvinen J, Bergfors T, Teeri T, Knowles JK, Jones TA, Science. 1990 Jul 27;249(4967):380-6. PMID:2377893
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